2b7s: Difference between revisions

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[[Image:2b7s.gif|left|200px]]<br /><applet load="2b7s" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2b7s.gif|left|200px]]
caption="2b7s, resolution 2.12&Aring;" />
 
'''R381K mutant of flavocytochrome c3'''<br />
{{Structure
|PDB= 2b7s |SIZE=350|CAPTION= <scene name='initialview01'>2b7s</scene>, resolution 2.12&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> and <scene name='pdbligand=FUM:FUMARIC ACID'>FUM</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1]
|GENE= FCC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=56812 Shewanella frigidimarina])
}}
 
'''R381K mutant of flavocytochrome c3'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2B7S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_frigidimarina Shewanella frigidimarina] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=FAD:'>FAD</scene> and <scene name='pdbligand=FUM:'>FUM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B7S OCA].  
2B7S is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Shewanella_frigidimarina Shewanella frigidimarina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B7S OCA].  


==Reference==
==Reference==
A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina., Pankhurst KL, Mowat CG, Rothery EL, Hudson JM, Jones AK, Miles CS, Walkinshaw MD, Armstrong FA, Reid GA, Chapman SK, J Biol Chem. 2006 Jul 21;281(29):20589-97. Epub 2006 May 12. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16699170 16699170]
A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina., Pankhurst KL, Mowat CG, Rothery EL, Hudson JM, Jones AK, Miles CS, Walkinshaw MD, Armstrong FA, Reid GA, Chapman SK, J Biol Chem. 2006 Jul 21;281(29):20589-97. Epub 2006 May 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16699170 16699170]
[[Category: Shewanella frigidimarina]]
[[Category: Shewanella frigidimarina]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: proton delivery]]
[[Category: proton delivery]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:35:02 2008''
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Revision as of 16:58, 20 March 2008

File:2b7s.gif


PDB ID 2b7s

Drag the structure with the mouse to rotate
, resolution 2.12Å
Ligands: , , and
Gene: FCC (Shewanella frigidimarina)
Activity: Succinate dehydrogenase, with EC number 1.3.99.1
Coordinates: save as pdb, mmCIF, xml



R381K mutant of flavocytochrome c3


OverviewOverview

The mechanism for fumarate reduction by the soluble fumarate reductase from Shewanella frigidimarina involves hydride transfer from FAD and proton transfer from the active-site acid, Arg-402. It has been proposed that Arg-402 forms part of a proton transfer pathway that also involves Glu-378 and Arg-381 but, unusually, does not involve any bound water molecules. To gain further insight into the importance of this proton pathway we have perturbed it by substituting Arg-381 by lysine and methionine and Glu-378 by aspartate. Although all the mutant enzymes retain measurable activities, there are orders-of-magnitude decreases in their k(cat) values compared with the wild-type enzyme. Solvent kinetic isotope effects show that proton transfer is rate-limiting in the wild-type and mutant enzymes. Proton inventories indicate that the proton pathway involves multiple exchangeable groups. Fast scan protein-film voltammetric studies on wild-type and R381K enzymes show that the proton transfer pathway delivers one proton per catalytic cycle and is not required for transporting the other proton, which transfers as a hydride from the reduced, protonated FAD. The crystal structures of E378D and R381M mutant enzymes have been determined to 1.7 and 2.1 A resolution, respectively. They allow an examination of the structural changes that disturb proton transport. Taken together, the results indicate that Arg-381, Glu-378, and Arg-402 form a proton pathway that is completely conserved throughout the fumarate reductase/succinate dehydrogenase family of enzymes.

About this StructureAbout this Structure

2B7S is a Single protein structure of sequence from Shewanella frigidimarina. Full crystallographic information is available from OCA.

ReferenceReference

A proton delivery pathway in the soluble fumarate reductase from Shewanella frigidimarina., Pankhurst KL, Mowat CG, Rothery EL, Hudson JM, Jones AK, Miles CS, Walkinshaw MD, Armstrong FA, Reid GA, Chapman SK, J Biol Chem. 2006 Jul 21;281(29):20589-97. Epub 2006 May 12. PMID:16699170

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